1998
DOI: 10.1021/la971352v
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Protein−DNA Double and Triple Layers:  Interaction of Biotinylated DNA Fragments with Solid Supported Streptavidin Layers

Abstract: The specific interaction of streptavidin with biotinylated lipids at the air-water interface leads to a formation of optically anisotropic two-dimensional streptavidin (2-D) crystals, where two of the original four biotin-binding sites remain free. These assembled streptavidin matrixes were used as a template for docking of double-stranded oligonucleotides biotinylated at a terminal or a centered position. A biotinylated lipid monolayer was deposited on an electrode of a quartz crystal microbalance (QCM), and … Show more

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Cited by 43 publications
(27 citation statements)
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“…Concentration-dependent measurements of the frequency shift together with the assumption of a linear relationship between frequency shift and mass load allow the determination of binding and rate constants of protein and peptide adsorption [49,60,62,[69][70][71]. Moreover, the QCM method has been evolved as a routine technique to control the quality of multilayers prepared by the Langmuir-Blodgett technique [72] or self-organization processes [68,[73][74][75][76][77][78][79][80].…”
Section: Adsorption Of Proteins At Functionalized Surfacesmentioning
confidence: 99%
“…Concentration-dependent measurements of the frequency shift together with the assumption of a linear relationship between frequency shift and mass load allow the determination of binding and rate constants of protein and peptide adsorption [49,60,62,[69][70][71]. Moreover, the QCM method has been evolved as a routine technique to control the quality of multilayers prepared by the Langmuir-Blodgett technique [72] or self-organization processes [68,[73][74][75][76][77][78][79][80].…”
Section: Adsorption Of Proteins At Functionalized Surfacesmentioning
confidence: 99%
“…Streptavidin has a well-known ability to assemble into optically anisotropic two-dimensional (2D) crystals at these interfaces [18][19][20][21] The prerequisite for the 2D protein crystallization is the mobility (lateral diffusion) of proteins at the interface. Furthermore, a streptavidin layer attached to a biotinylated lipid monolayer can itself act as a receptor template for other biotin-functionalized molecules [22,23].…”
Section: Introductionmentioning
confidence: 99%
“…The presented method takes advantage of these characteristics, using the CD3 and CD4 biomarkers to distinguish the T helper cells (targets) from the B cells. The tight binding affinity of biotin-streptavidin [15][16][17] enables linkage to the target T helper cells through biotinylated anti-CD3 antibody and HRP-stv. The membranes of the T helper cells thus conjugated with anti-human CD4-MNPs through the antigenantibody reaction, yielding the MNP-bound T helper cells.…”
Section: Proof Of Conceptmentioning
confidence: 99%